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PDBsum entry 3vyj
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Carbohydrate binding protein
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PDB id
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3vyj
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PDB id:
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| Name: |
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Carbohydrate binding protein
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Title:
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Crystal structure of c-type lectin domain of murine dendritic cell inhibitory receptor 2 (apo form)
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Structure:
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C-type lectin domain family 4, member a4. Chain: a. Fragment: unp residues 107-233. Synonym: dendritic cell immunoreceptor-2, dendritic cell inhibitory receptor 2, mcg1050915, protein clec4a4. Engineered: yes
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Source:
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Mus musculus. Mouse. Organism_taxid: 10090. Gene: dcir2. Expressed in: escherichia coli. Expression_system_taxid: 562.
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Resolution:
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2.15Å
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R-factor:
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0.237
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R-free:
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0.272
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Authors:
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M.Nagae,K.Yamanaka,S.Hanashima,A.Ikeda,T.Satoh,N.Matsumoto, K.Yamamoto,Y.Yamaguchi
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Key ref:
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M.Nagae
et al.
(2013).
Recognition of bisecting N-acetylglucosamine: structural basis for asymmetric interaction with the mouse lectin dendritic cell inhibitory receptor 2.
J Biol Chem,
288,
33598-33610.
PubMed id:
DOI:
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Date:
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26-Sep-12
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Release date:
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02-Oct-13
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PROCHECK
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Headers
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References
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Q5YIR8
(Q5YIR8_MOUSE) -
C-type lectin domain family 4, member a4 from Mus musculus
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Seq:
Struc:
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236 a.a.
128 a.a.*
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Key: |
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PfamA domain |
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Secondary structure |
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CATH domain |
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*
PDB and UniProt seqs differ
at 1 residue position (black
cross)
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DOI no:
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J Biol Chem
288:33598-33610
(2013)
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PubMed id:
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Recognition of bisecting N-acetylglucosamine: structural basis for asymmetric interaction with the mouse lectin dendritic cell inhibitory receptor 2.
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M.Nagae,
K.Yamanaka,
S.Hanashima,
A.Ikeda,
K.Morita-Matsumoto,
T.Satoh,
N.Matsumoto,
K.Yamamoto,
Y.Yamaguchi.
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ABSTRACT
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Dendritic cell inhibitory receptor 2 (DCIR2) is a C-type lectin expressed on
classical dendritic cells. We recently identified the unique ligand specificity
of mouse DCIR2 (mDCIR2) toward biantennary complex-type glycans containing
bisecting N-acetylglucosamine (GlcNAc). Here, we report the crystal structures
of the mDCIR2 carbohydrate recognition domain in unliganded form as well as in
complex with an agalactosylated complex-type N-glycan unit carrying a bisecting
GlcNAc residue. Bisecting GlcNAc and the α1-3 branch of the biantennary
oligosaccharide asymmetrically interact with canonical and non-canonical mDCIR2
residues. Ligand-protein interactions occur directly through
mDCIR2-characteristic amino acid residues as well as via a calcium ion and water
molecule. Our structural and biochemical data elucidate for the first time the
unique binding mode of mDCIR2 for bisecting GlcNAc-containing glycans, a mode
that contrasts sharply with that of other immune C-type lectin receptors such as
DC-SIGN.
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Links
